Chapter 3 - Enzymes 2024
Unit 3 AOS1 MW Biology: Chapter Overview
Chapter 3: Enzymes
3A: Introducing Enzymes
3B: Factors Affecting Enzymes
Study Design
Proteins
Diverse group forming an organism's proteome
Includes enzymes as key catalysts in biochemical pathways
Factors Impacting Enzyme Function:
Temperature
pH
Concentration levels
Competitive and non-competitive enzyme inhibitors
Role of Enzymes and Coenzymes
Facilitate steps in photosynthesis and cellular respiration
3A: Introducing Enzymes
Definition of Enzymes
Organic catalysts that speed up biochemical reactions
Bind to substrates (reactants undergoing reaction)
Active Site
Each enzyme contains a specific active site complementary to the substrate's shape
Forms an enzyme-substrate complex upon binding, which leads to a conformational change.
Reaction Process
Substrate undergoes a chemical transformation to yield products
Specific Examples
Enzyme Example: Maltase
Substrate: Maltose
Products: Glucose
Enzyme-Substrate Interaction
An enzyme's active site allows binding of specific substrates, facilitating unique reactions
Characteristics of Enzymes
Reusable
Enzymes are not consumed in reactions and can catalyze multiple reactions
Specificity
Each enzyme typically acts upon one specific substrate
Catalysis
Enzymes lower activation energy required for reactions
Enzyme Functioning
Conformational Change
Upon substrate binding:
Enzyme changes shape to enhance fit with substrate
Results in successful product formation
Activation Energy
Definition:
Minimum energy required for a reaction
Effect of Enzymes:
Enzymes lower the activation energy, facilitating faster reactions
Types of Reactions
Catabolic Reactions
Larger molecules break down into smaller ones, releasing energy
Anabolic Reactions
Smaller molecules combine to form larger ones, storing energy
3B: Factors that Affect Enzymes
Temperature Impact on Enzyme Activity
Too Cold: Reduced activity due to slower molecular movement
Optimal Temperature: Increased kinetic energy leading to more substrate interactions
Too Hot: Risk of denaturation, where enzymes lose shape and can no longer function
pH Influence
Variations can lead to enzyme denaturation
Optimal pH varies by enzyme type (e.g., pepsin in stomach has pH of ~1.5-2)
Concentration Effects
Substrate Concentration: Increased concentration elevates reaction rates until saturation is reached
Enzyme Concentration: Higher enzyme concentrations lead to faster reactions until enzyme saturation occurs
Inhibition Types
Competitive Inhibition: Inhibitor blocks active site, preventing substrate binding
Non-competitive Inhibition: Inhibitor binds elsewhere, altering active site shape
Coenzymes
Assistance in Reactions:
Cofactors are needed for some enzyme reactions; coenzymes are organic cofactors
Coenzymes assist by donating energy/molecules that cycle through reactions
Example of a Coenzyme: ATP
Function: Main energy carrier in cells
Process:
Releases energy by losing a phosphate group (ATP to ADP)
Can return to ATP through rephosphorylation
Exam Strategies
Read questions carefully
Highlight key information in prompts
Assess question requirements based on mark allocation
Ensure response length meets expected answers, based on allocated marks